Issue 15, 2021

Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region

Abstract

Proteoglycans (PGs) play important roles in many biological processes including tumor progression, cell adhesion, and regulation of growth factor activities. With glycosaminoglycan chains attached to the core proteins in nature, PGs are highly challenging synthetic targets due to the difficulties in integrating the sulfated glycans with the peptide backbone. To expedite the synthesis, herein, the utility of human xylosyltransferase I (XT-I), the enzyme responsible for initiating PG synthesis, has been explored. XT-I was found to be capable of efficiently installing the xylose unit onto a variety of peptide structures on mg scales. Furthermore, an unnatural sugar, i.e., 6-azidoglucose can be transferred by XT-I introducing a reactive handle onto the glycopeptide for selective functionalization. XT-I can be coupled with β-4-galactosyl transferase-7 for one pot synthesis of glycopeptides bearing galactose-xylose disaccharide, paving the way toward efficient chemoenzymatic synthesis of PG glycopeptides and glycoproteins.

Graphical abstract: Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region

Supplementary files

Article information

Article type
Communication
Submitted
20 fev 2021
Accepted
22 mar 2021
First published
22 mar 2021

Org. Biomol. Chem., 2021,19, 3374-3378

Exploration of human xylosyltransferase for chemoenzymatic synthesis of proteoglycan linkage region

J. Gao, P. Lin, S. T. Nick, K. Liu, K. Yu, E. Hohenester and X. Huang, Org. Biomol. Chem., 2021, 19, 3374 DOI: 10.1039/D1OB00317H

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